ID   KLK3_HUMAN              Reviewed;         261 AA.
AC   P07288; C9JXH3; G3V0H4; G3XAE3; Q15096; Q16272; Q86TG8; Q8IXI4;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   27-MAR-2024, entry version 232.
DE   RecName: Full=Prostate-specific antigen;
DE            Short=PSA;
DE            EC=3.4.21.77;
DE   AltName: Full=Gamma-seminoprotein;
DE            Short=Seminin;
DE   AltName: Full=Kallikrein-3;
DE   AltName: Full=P-30 antigen;
DE   AltName: Full=Semenogelase;
DE   Flags: Precursor;
GN   Name=KLK3; Synonyms=APS;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 4-238
RP   (ISOFORM 2), AND ALTERNATIVE SPLICING.
RC   TISSUE=Prostate;
RX   PubMed=2436946; DOI=10.1016/0014-5793(87)80078-9;
RA   Lundwall A., Lilja H.;
RT   "Molecular cloning of human prostate specific antigen cDNA.";
RL   FEBS Lett. 214:317-322(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Prostate;
RX   PubMed=2467258; DOI=10.1093/nar/17.5.2137;
RA   Digby M.R., Zhang X.Y., Richard R.I.;
RT   "Human prostate specific antigen (PSA) gene: structure and linkage to the
RT   kallikrein-like gene, hGK-1.";
RL   Nucleic Acids Res. 17:2137-2137(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2471958; DOI=10.1093/nar/17.10.3981;
RA   Klobeck H.-G., Combriato G., Schulz P., Arbusow V., Fittler F.;
RT   "Genomic sequence of human prostate specific antigen (PSA).";
RL   Nucleic Acids Res. 17:3981-3981(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leukocyte;
RX   PubMed=2472789; DOI=10.1016/0006-291x(89)91362-4;
RA   Lundwall A.;
RT   "Characterization of the gene for prostate-specific antigen, a human
RT   glandular kallikrein.";
RL   Biochem. Biophys. Res. Commun. 161:1151-1159(1989).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Prostate;
RX   PubMed=2470373; DOI=10.1016/0006-291x(89)92520-5;
RA   Henttu P., Vihko P.;
RT   "cDNA coding for the entire human prostate specific antigen shows high
RT   homologies to the human tissue kallikrein genes.";
RL   Biochem. Biophys. Res. Commun. 160:903-910(1989).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Prostate;
RX   PubMed=2466464; DOI=10.1016/0006-291x(89)92409-1;
RA   Riegman P.H.J., Vlietstra R.J., van der Korput J.A.G.M., Romijn J.C.,
RA   Trapman J.;
RT   "Characterization of the prostate-specific antigen gene: a novel human
RT   kallikrein-like gene.";
RL   Biochem. Biophys. Res. Commun. 159:95-102(1989).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Prostate;
RX   PubMed=8677566; DOI=10.1016/s0090-4295(96)00060-x;
RA   Baffa R., Moreno J.G., Monne M., Veronese M.L., Gomella L.G.;
RT   "A comparative analysis of prostate-specific antigen gene sequence in
RT   benign and malignant prostate tissue.";
RL   Urology 47:795-800(1996).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11054574; DOI=10.1016/s0378-1119(00)00382-6;
RA   Gan L., Lee I., Smith R., Argonza-Barrett R., Lei H., McCuaig J., Moss P.,
RA   Paeper B., Wang K.;
RT   "Sequencing and expression analysis of the serine protease gene cluster
RT   located in chromosome 19q13 region.";
RL   Gene 257:119-130(2000).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND ALTERNATIVE SPLICING.
RC   TISSUE=Prostate;
RA   Heuze-Vourc'h N., Courty Y.;
RT   "Complex alternative splicing of the hKLK3 gene coding for the tumour
RT   marker PSA (prostate-specific-antigen).";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC   TISSUE=PNS, Prostate, and Sciatic nerve;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-176 (ISOFORM 1).
RX   PubMed=7527295;
RA   Monne M., Croce C.M., Yu H., Diamandis E.P.;
RT   "Molecular characterization of prostate-specific antigen messenger RNA
RT   expressed in breast tumors.";
RL   Cancer Res. 54:6344-6347(1994).
RN   [15]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 17-261 (ISOFORM 1).
RX   PubMed=2456523; DOI=10.1093/nar/16.13.6226;
RA   Schulz P., Stucka R., Feldmann H., Combriato G., Klobeck H.-G., Fittler F.;
RT   "Sequence of a cDNA clone encompassing the complete mature human prostate
RT   specific antigen (PSA) and an unspliced leader sequence.";
RL   Nucleic Acids Res. 16:6226-6226(1988).
RN   [16]
RP   PROTEIN SEQUENCE OF 25-261.
RX   PubMed=2422647; DOI=10.1073/pnas.83.10.3166;
RA   Watt K.W.K., Lee P.J., M'Timkulu T., Chan W.P., Loor R.;
RT   "Human prostate-specific antigen: structural and functional similarity with
RT   serine proteases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:3166-3170(1986).
RN   [17]
RP   PROTEIN SEQUENCE OF 25-261.
RX   PubMed=3691515; DOI=10.1111/j.1432-1033.1987.tb13674.x;
RA   Schaller J., Akiyama K., Tsuda R., Hara M., Marti T., Rickli E.E.;
RT   "Isolation, characterization and amino-acid sequence of gamma-
RT   seminoprotein, a glycoprotein from human seminal plasma.";
RL   Eur. J. Biochem. 170:111-120(1987).
RN   [18]
RP   PROTEIN SEQUENCE OF 18-32.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [19]
RP   PROTEIN SEQUENCE OF 126-138, AND VARIANT ILE-132.
RX   PubMed=23842001; DOI=10.1074/mcp.m113.028365;
RA   Vegvari A., Sjodin K., Rezeli M., Malm J., Lilja H., Laurell T.,
RA   Marko-Varga G.;
RT   "Identification of a novel proteoform of prostate specific antigen (SNP-
RT   L132I) in clinical samples by multiple reaction monitoring.";
RL   Mol. Cell. Proteomics 12:2761-2773(2013).
RN   [20]
RP   ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5.
RX   PubMed=1725227; DOI=10.1016/0049-3848(91)90002-e;
RA   Espana F., Gilabert J., Estelles A., Romeu A., Aznar J., Cabo A.;
RT   "Functionally active protein C inhibitor/plasminogen activator inhibitor-3
RT   (PCI/PAI-3) is secreted in seminal vesicles, occurs at high concentrations
RT   in human seminal plasma and complexes with prostate-specific antigen.";
RL   Thromb. Res. 64:309-320(1991).
RN   [21]
RP   3D-STRUCTURE MODELING.
RX   PubMed=7535613; DOI=10.1002/pro.5560031116;
RA   Villoutreix B.O., Getzoff E.D., Griffin J.H.;
RT   "A structural model for the prostate disease marker, human prostate-
RT   specific antigen.";
RL   Protein Sci. 3:2033-2044(1994).
RN   [22]
RP   3D-STRUCTURE MODELING.
RX   PubMed=9751643; DOI=10.1016/s1074-5521(98)90004-7;
RA   Coombs G.S., Bergstrom R.C., Pellequer J.L., Baker S.I., Navre M.,
RA   Smith M.M., Tainer J.A., Madison E.L., Corey D.R.;
RT   "Substrate specificity of prostate-specific antigen (PSA).";
RL   Chem. Biol. 5:475-488(1998).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (2.83 ANGSTROMS) OF 25-261 IN COMPLEX WITH SUBSTRATE
RP   AND ACTIVATING ANTIBODY, ACTIVITY REGULATION, ACTIVE SITE, AND DISULFIDE
RP   BONDS.
RX   PubMed=18187150; DOI=10.1016/j.jmb.2007.11.052;
RA   Menez R., Michel S., Muller B.H., Bossus M., Ducancel F.,
RA   Jolivet-Reynaud C., Stura E.A.;
RT   "Crystal structure of a ternary complex between human prostate-specific
RT   antigen, its substrate acyl intermediate and an activating antibody.";
RL   J. Mol. Biol. 376:1021-1033(2008).
CC   -!- FUNCTION: Hydrolyzes semenogelin-1 thus leading to the liquefaction of
CC       the seminal coagulum.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: -Tyr-|-Xaa-.; EC=3.4.21.77;
CC   -!- ACTIVITY REGULATION: Inhibited by SERPINA5. Activity is strongly
CC       inhibited by Zn2+, 100 times more abundant in semen than in serum. This
CC       inhibition is relieved by exposure to semenogelins, which are avid zinc
CC       binders. {ECO:0000269|PubMed:1725227, ECO:0000269|PubMed:18187150}.
CC   -!- SUBUNIT: Forms a heterodimer with SERPINA5.
CC       {ECO:0000269|PubMed:18187150}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=P07288-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P07288-2; Sequence=VSP_045786;
CC       Name=3;
CC         IsoId=P07288-3; Sequence=VSP_046169, VSP_046171;
CC       Name=4;
CC         IsoId=P07288-4; Sequence=VSP_046169, VSP_046170;
CC       Name=5;
CC         IsoId=P07288-5; Sequence=VSP_047643;
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD14185.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA32124.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Prostate-specific antigen entry;
CC       URL="https://en.wikipedia.org/wiki/Prostate_specific_antigen";
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DR   EMBL; M21896; AAA59996.1; -; mRNA.
DR   EMBL; X05332; CAA28947.1; -; mRNA.
DR   EMBL; X13940; CAA32123.1; -; Genomic_DNA.
DR   EMBL; X13941; CAA32124.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X13942; CAB46487.1; -; Genomic_DNA.
DR   EMBL; X13943; CAA32126.1; -; Genomic_DNA.
DR   EMBL; X13944; CAA32127.1; -; Genomic_DNA.
DR   EMBL; X14810; CAA32915.1; -; Genomic_DNA.
DR   EMBL; M27274; AAA60192.1; -; Genomic_DNA.
DR   EMBL; M26663; AAA58802.1; -; mRNA.
DR   EMBL; M24543; AAA60193.1; -; Genomic_DNA.
DR   EMBL; U17040; AAA56764.1; -; mRNA.
DR   EMBL; AF243527; AAG33355.1; -; Genomic_DNA.
DR   EMBL; AJ512346; CAD54617.1; -; mRNA.
DR   EMBL; BT019862; AAV38665.1; -; mRNA.
DR   EMBL; AC011523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471135; EAW71929.1; -; Genomic_DNA.
DR   EMBL; CH471135; EAW71930.1; -; Genomic_DNA.
DR   EMBL; CH471135; EAW71936.1; -; Genomic_DNA.
DR   EMBL; BC005307; AAH05307.1; -; mRNA.
DR   EMBL; BC050595; AAH50595.2; -; mRNA.
DR   EMBL; BC056665; AAH56665.1; -; mRNA.
DR   EMBL; BF679511; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BQ932072; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; S75755; AAD14185.1; ALT_INIT; mRNA.
DR   EMBL; X07730; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS12807.1; -. [P07288-1]
DR   CCDS; CCDS33083.1; -. [P07288-2]
DR   CCDS; CCDS46155.1; -. [P07288-3]
DR   PIR; A32297; A32297.
DR   RefSeq; NP_001025218.1; NM_001030047.1. [P07288-2]
DR   RefSeq; NP_001025219.1; NM_001030048.1. [P07288-3]
DR   RefSeq; NP_001639.1; NM_001648.2. [P07288-1]
DR   PDB; 2ZCH; X-ray; 2.83 A; P=25-261.
DR   PDB; 2ZCK; X-ray; 3.10 A; P=25-261.
DR   PDB; 2ZCL; X-ray; 3.25 A; P=25-261.
DR   PDB; 3QUM; X-ray; 3.20 A; P/Q=25-261.
DR   PDBsum; 2ZCH; -.
DR   PDBsum; 2ZCK; -.
DR   PDBsum; 2ZCL; -.
DR   PDBsum; 3QUM; -.
DR   AlphaFoldDB; P07288; -.
DR   SMR; P07288; -.
DR   BioGRID; 106850; 62.
DR   CORUM; P07288; -.
DR   IntAct; P07288; 10.
DR   MINT; P07288; -.
DR   STRING; 9606.ENSP00000314151; -.
DR   BindingDB; P07288; -.
DR   ChEMBL; CHEMBL2099; -.
DR   DrugBank; DB04839; Cyproterone acetate.
DR   DrugBank; DB16019; Gallium Ga-68 gozetotide.
DR   DrugBank; DB16778; Lutetium Lu-177 vipivotide tetraxetan.
DR   DrugBank; DB02998; Metribolone.
DR   DrugBank; DB00834; Mifepristone.
DR   GuidetoPHARMACOLOGY; 2373; -.
DR   Allergome; 2836; Hom s PSA.
DR   MEROPS; S01.162; -.
DR   GlyConnect; 666; 57 N-Linked glycans (1 site).
DR   GlyConnect; 790; 167 N-Linked glycans (1 site).
DR   GlyCosmos; P07288; 1 site, 176 glycans.
DR   GlyGen; P07288; 1 site, 192 N-linked glycans (1 site).
DR   iPTMnet; P07288; -.
DR   PhosphoSitePlus; P07288; -.
DR   SwissPalm; P07288; -.
DR   BioMuta; KLK3; -.
DR   DMDM; 130989; -.
DR   CPTAC; CPTAC-1296; -.
DR   CPTAC; CPTAC-1476; -.
DR   jPOST; P07288; -.
DR   MassIVE; P07288; -.
DR   MaxQB; P07288; -.
DR   PaxDb; 9606-ENSP00000314151; -.
DR   PeptideAtlas; P07288; -.
DR   ProteomicsDB; 12120; -.
DR   ProteomicsDB; 32197; -.
DR   ProteomicsDB; 33725; -.
DR   ProteomicsDB; 51977; -. [P07288-1]
DR   ABCD; P07288; 9 sequenced antibodies.
DR   Antibodypedia; 743; 2757 antibodies from 51 providers.
DR   DNASU; 354; -.
DR   Ensembl; ENST00000326003.7; ENSP00000314151.1; ENSG00000142515.16. [P07288-1]
DR   Ensembl; ENST00000360617.7; ENSP00000353829.2; ENSG00000142515.16. [P07288-2]
DR   Ensembl; ENST00000593997.5; ENSP00000472907.1; ENSG00000142515.16. [P07288-5]
DR   Ensembl; ENST00000595952.5; ENSP00000471155.1; ENSG00000142515.16. [P07288-3]
DR   GeneID; 354; -.
DR   KEGG; hsa:354; -.
DR   MANE-Select; ENST00000326003.7; ENSP00000314151.1; NM_001648.2; NP_001639.1.
DR   UCSC; uc002ptr.2; human. [P07288-1]
DR   AGR; HGNC:6364; -.
DR   CTD; 354; -.
DR   DisGeNET; 354; -.
DR   GeneCards; KLK3; -.
DR   HGNC; HGNC:6364; KLK3.
DR   HPA; ENSG00000142515; Tissue enriched (prostate).
DR   MIM; 176820; gene.
DR   neXtProt; NX_P07288; -.
DR   OpenTargets; ENSG00000142515; -.
DR   PharmGKB; PA164741810; -.
DR   VEuPathDB; HostDB:ENSG00000142515; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT01020000230389; -.
DR   HOGENOM; CLU_006842_1_1_1; -.
DR   InParanoid; P07288; -.
DR   OMA; IGGRECL; -.
DR   OrthoDB; 4629979at2759; -.
DR   PhylomeDB; P07288; -.
DR   TreeFam; TF331065; -.
DR   BRENDA; 3.4.21.77; 2681.
DR   PathwayCommons; P07288; -.
DR   Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR   SignaLink; P07288; -.
DR   SIGNOR; P07288; -.
DR   BioGRID-ORCS; 354; 8 hits in 1149 CRISPR screens.
DR   ChiTaRS; KLK3; human.
DR   EvolutionaryTrace; P07288; -.
DR   GeneWiki; Prostate-specific_antigen; -.
DR   GenomeRNAi; 354; -.
DR   Pharos; P07288; Tclin.
DR   PRO; PR:P07288; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P07288; Protein.
DR   Bgee; ENSG00000142515; Expressed in prostate gland and 123 other cell types or tissues.
DR   ExpressionAtlas; P07288; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IMP:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IMP:UniProtKB.
DR   GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; NAS:UniProtKB.
DR   GO; GO:0002803; P:positive regulation of antibacterial peptide production; IDA:UniProtKB.
DR   GO; GO:0019538; P:protein metabolic process; TAS:Reactome.
DR   GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24271; KALLIKREIN-RELATED; 1.
DR   PANTHER; PTHR24271:SF73; PROSTATE-SPECIFIC ANTIGEN; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
DR   Genevisible; P07288; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   PROPEP          18..24
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:2422647,
FT                   ECO:0000269|PubMed:3691515"
FT                   /id="PRO_0000027931"
FT   CHAIN           25..261
FT                   /note="Prostate-specific antigen"
FT                   /id="PRO_0000027932"
FT   DOMAIN          25..258
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        65
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:18187150"
FT   ACT_SITE        120
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:18187150"
FT   ACT_SITE        213
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:18187150"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        31..173
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:18187150"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:18187150"
FT   DISULFID        152..219
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:18187150"
FT   DISULFID        184..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:18187150"
FT   DISULFID        209..234
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:18187150"
FT   VAR_SEQ         69
FT                   /note="N -> K (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_046169"
FT   VAR_SEQ         70..261
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_046170"
FT   VAR_SEQ         70..112
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_046171"
FT   VAR_SEQ         211..261
FT                   /note="GDSGGPLVCNGVLQGITSWGSEPCALPERPSLYTKVVHYRKWIKDTIVANP
FT                   -> WVILITELTMPALPMVLHGSLVPWRGGV (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:2436946"
FT                   /id="VSP_045786"
FT   VAR_SEQ         211..260
FT                   /note="GDSGGPLVCNGVLQGITSWGSEPCALPERPSLYTKVVHYRKWIKDTIVAN
FT                   -> VSHPYSQDLEGKGEWG (in isoform 5)"
FT                   /evidence="ECO:0000303|Ref.9"
FT                   /id="VSP_047643"
FT   VARIANT         32
FT                   /note="E -> K (in dbSNP:rs2271092)"
FT                   /id="VAR_021941"
FT   VARIANT         132
FT                   /note="L -> I (in dbSNP:rs2003783)"
FT                   /evidence="ECO:0000269|PubMed:23842001"
FT                   /id="VAR_021942"
FT   VARIANT         179
FT                   /note="I -> T (in dbSNP:rs17632542)"
FT                   /id="VAR_051852"
FT   CONFLICT        64
FT                   /note="A -> T (in Ref. 15)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69
FT                   /note="N -> KC (in Ref. 6; AAA60193)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        94
FT                   /note="H -> T (in Ref. 16; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        136
FT                   /note="V -> M (in Ref. 15)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165..168
FT                   /note="FLTP -> HLLYDQM (in Ref. 16; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        175
FT                   /note="D -> Q (in Ref. 16; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          39..56
FT                   /evidence="ECO:0007829|PDB:2ZCH"
FT   STRAND          59..62
FT                   /evidence="ECO:0007829|PDB:2ZCH"
FT   HELIX           64..66
FT                   /evidence="ECO:0007829|PDB:2ZCH"
FT   STRAND          72..76
FT                   /evidence="ECO:0007829|PDB:2ZCH"
FT   STRAND          78..82
FT                   /evidence="ECO:0007829|PDB:2ZCH"
FT   STRAND          88..97
FT                   /evidence="ECO:0007829|PDB:2ZCH"
FT   HELIX           103..106
FT                   /evidence="ECO:0007829|PDB:2ZCH"
FT   STRAND          107..110
FT                   /evidence="ECO:0007829|PDB:2ZCH"
FT   STRAND          122..128
FT                   /evidence="ECO:0007829|PDB:2ZCH"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:2ZCK"
FT   STRAND          151..157
FT                   /evidence="ECO:0007829|PDB:2ZCH"
FT   STRAND          160..164
FT                   /evidence="ECO:0007829|PDB:2ZCH"
FT   STRAND          172..179
FT                   /evidence="ECO:0007829|PDB:2ZCH"
FT   HELIX           181..187
FT                   /evidence="ECO:0007829|PDB:2ZCH"
FT   STRAND          189..191
FT                   /evidence="ECO:0007829|PDB:2ZCH"
FT   STRAND          196..200
FT                   /evidence="ECO:0007829|PDB:2ZCH"
FT   STRAND          216..229
FT                   /evidence="ECO:0007829|PDB:2ZCH"
FT   STRAND          232..235
FT                   /evidence="ECO:0007829|PDB:2ZCL"
FT   STRAND          241..245
FT                   /evidence="ECO:0007829|PDB:2ZCH"
FT   HELIX           246..249
FT                   /evidence="ECO:0007829|PDB:2ZCH"
FT   HELIX           250..258
FT                   /evidence="ECO:0007829|PDB:2ZCH"
SQ   SEQUENCE   261 AA;  28741 MW;  AE9E732AF872141A CRC64;
     MWVPVVFLTL SVTWIGAAPL ILSRIVGGWE CEKHSQPWQV LVASRGRAVC GGVLVHPQWV
     LTAAHCIRNK SVILLGRHSL FHPEDTGQVF QVSHSFPHPL YDMSLLKNRF LRPGDDSSHD
     LMLLRLSEPA ELTDAVKVMD LPTQEPALGT TCYASGWGSI EPEEFLTPKK LQCVDLHVIS
     NDVCAQVHPQ KVTKFMLCAG RWTGGKSTCS GDSGGPLVCN GVLQGITSWG SEPCALPERP
     SLYTKVVHYR KWIKDTIVAN P
//